Virus Details


VHFID5028

Host Factor Information

Gene Name SDC2
HF Protein Name Syndecan-2
HF Function Involves in HTLV-1 Entry
Uniprot ID P34741
Protein Sequence View Fasta Sequence
NCBI Gene ID 6383
Host Factor (HF) Name in Paper HSPG
Gene synonyms HSPG1
Ensemble Gene ID ENSG00000169439
Ensemble Transcript ENST00000302190
KEGG ID Go to KEGG Database
Gene Ontology ID(s) GO:0001523, GO:0005788, GO:0005796, GO:0005886, GO:0006024, GO:0006027, GO:0008218, GO:0009986, GO:0016021, GO:0016477, GO:0030165, GO:0030203, GO:0031012, GO:0042802, GO:0043202, GO:0043687, GO:0044267, GO:0048013, GO:0048813, GO:0048814, GO:0050900,
MINT ID P34741
STRING Click to see interaction map
GWAS Analysis Click to see gwas analysis
OMIM ID 142460
PANTHER ID PTHR10915;PTHR10915:SF6
PDB ID(s) N.A.,
pfam ID PF01034,
Drug Bank ID DB00020,
ChEMBL ID N.A.
Organism Homo sapiens (Human)

Pathogen Information

Virus Name Human T-lymphotropic virus1
Virus Short Name HTLV-I
Order Unassigned
Virus Family Retroviridae
Virus Subfamily Orthoretrovirinae
Genus Deltaretrovirus
Species Human T-lymphotropic virus 1
Host Vertebrates
Cell Tropism Lymphocytes
Associated Disease Adult t-cell leukemia
Mode of Transmission Sexual contact, maternal-neonatal
VIPR DB link N.A.
ICTV DB link https://talk.ictvonline.org/ictv-reports/ictv_9th_report/reverse-transcribing-dna-and-rna-viruses-2011/w/rt_viruses/161/retroviridae
Virus Host DB link http://www.genome.jp/virushostdb/view/?virus_lineage=Retroviridae

Publication Information

Paper Title Heparan sulfate proteoglycans mediate attachment and entry of human T-Cell leukemia virus type 1 virions into CD4+ T cells
Author's Name Kathryn S. Jones, Cari Petrow-Sadowski, Daniel C. Bertolette, Ying Huang, and Francis W. Ruscetti
Journal Name Journal Of Virology
Pubmed ID 16188972
Abstract Heparan sulfate proteoglycans (HSPGs) are used by a number of viruses to facilitate entry into host cells. For the retrovirus human T-cell leukemia virus type 1 (HTLV-1), it has recently been reported that HSPGs are critical for efficient binding of soluble HTLV-1 SU and the entry of HTLV pseudotyped viruses into non-T cells. However, the primary in vivo targets of HTLV-1, CD4(+) T cells, have been reported to express low or undetectable levels of HSPGs. For this study, we reexamined the expression of HSPGs in CD4(+) T cells and examined their role in HTLV-1 attachment and entry. We observed that while quiescent primary CD4(+) T cells do not express detectable levels of HSPGs, HSPGs are expressed on primary CD4(+) T cells following immune activation. Enzymatic modification of HSPGs on the surfaces of either established CD4(+) T-cell lines or primary CD4(+) T cells dramatically reduced the binding of both soluble HTLV-1 SU and HTLV-1 virions. HSPGs also affected the efficiency of HTLV-1 entry, since blocking the interaction with HSPGs markedly reduced both the internalization of HTLV-1 virions and the titer of HTLV-1 pseudotyped viral infection in CD4(+) T cells. Thus, HSPGs play a critical role in the binding and entry of HTLV-1 into CD4(+) T cells.
Used Model MOLT4 and SupT1 cell lines
DOI 10.1128/JVI.79.20.12692-12702.2005